VEGFR2 Fc Human

Vascular Endothelial Growth Factor Receptor-2 Fc Chimera Human Recombinant
Cat. No.
BT21829
Source
Insect Cells.
Synonyms
KDR D1-7, sKDR D1-7, Kinase insert domain receptor, Protein-tyrosine kinase receptor Flk-1, CD309, type III receptor tyrosine kinase, FLK1, VEGFR-2.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

Soluble VEGFR2 Fc Human Recombinant fused with the Fc part of human IgG1 produced in baculovirus is a disulfide-linked homodimeric, glycosylated, polypeptide containing 968 amino acids and having a molecular mass of 145 kDa. The soluble receptor protein contains only the first 7 extracellular domains, which contain all the information necessary for ligand binding.
The sKDR Fc Chimera is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Endothelial cells exclusively express three vascular endothelial growth factor (VEGF) receptors, categorized as receptor tyrosine kinases (RTKs). These receptors, VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4), are primarily found on endothelial cells, with VEGFR-1 also present on monocytes. Each receptor comprises seven immunoglobulin-like extracellular domains, a single transmembrane region, and an intracellular split tyrosine kinase domain. VEGFR-2 exhibits a lower affinity for VEGF compared to Flt-1 but demonstrates higher signaling activity, primarily driving endothelial cell proliferation through its mitogenic activity. Notably, the flt-1 gene undergoes differential splicing, resulting in a soluble variant of VEGFR-1 (sVEGFR-1), while no naturally occurring secreted forms of VEGFR-2 have been identified. Heparin plays a crucial role in facilitating the binding of VEGF165 to VEGFR-2.
Description
Soluble VEGFR2 Fc Human Recombinant, fused with the Fc portion of human IgG1 and produced in a baculovirus expression system, is a disulfide-linked homodimeric glycoprotein. With a molecular weight of 145 kDa, this protein consists of 968 amino acids. It comprises the first seven extracellular domains responsible for ligand binding. Purification of the sKDR Fc Chimera is achieved through proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
The KDR fusion protein undergoes lyophilization from a sterile solution (1 mg/ml) containing 1xPBS at pH 7.2.
Solubility
To reconstitute the lyophilized VEGFR2, it is recommended to dissolve it in sterile water at a concentration of at least 50 µg/ml. Further dilutions can be prepared in other aqueous solutions.
Stability
Lyophilized VEGFR-2 Fc/Chimera protein remains stable at room temperature for up to 3 weeks; however, it is recommended to store it desiccated below -18°C. Once reconstituted, FLK1 should be stored at 4°C for 2-7 days. For long-term storage, freezing below -18°C is advised. To enhance stability during prolonged storage, the addition of a carrier protein (0.1% HSA or BSA) is recommended. It's essential to avoid repeated freeze-thaw cycles.
Purity
The purity of the protein is determined to be greater than 90.0% as assessed by SDS-PAGE analysis.
Biological Activity
The biological activity of sVEGFR2/Fc is evaluated based on its capacity to inhibit VEGF-dependent proliferation of human umbilical vein endothelial cells.
Synonyms
KDR D1-7, sKDR D1-7, Kinase insert domain receptor, Protein-tyrosine kinase receptor Flk-1, CD309, type III receptor tyrosine kinase, FLK1, VEGFR-2.
Source
Insect Cells.
Amino Acid Sequence

ASVGLPSVSL DLPRLSIQKD ILTIKANTTL QITCRGQRDL DWLWPNNQSG SEQRVEVTEC SDGLFCKTLT IPKVIGNDTG AYKCFYRETD LASVIYVYVQ DYRSPFIASV SDQHGVVYIT ENKNKTVVIP CLGSISNLNV SLCARYPEKR FVPDGNRISW DSKKGFTIPS YMISYAGMVF CEAKINDESY QSIMYIVVVV GYRIYDVVLS PSHGIELSVG EKLVLNCTAR TELNVGIDFN WEYPSSKHQH KKLVNRDLKT QSGSEMKKFL STLTIDGVTR SDQGLYTCAA SSGLMTKKNS TFVRVHEKPF VAFGSGMESL VEATVGERVR IPAKYLGYPP PEIKWYKNGI PLESNHTIKA GHVLTIMEVS ERDTGNYTVI LTNPISKEKQ SHVVSLVVYV PPQIGEKSLI SPVDSYQYGT TQTLTCTVYA IPPPHHIHWY WQLEEECANE PSQAVSVTNP YPCEEWRSVE DFQGGNKIEV NKNQFALIEG KNKTVSTLVI QAANVSALYK CEAVNKVGRG ERVISFHVTR GPEITLQPDM QPTEQESVSL WCTADRSTFE NLTWYKLGPQ PLPIHVGELP TPVCKNLDTL WKLNATMFSN STNDILIMEL KNASLQDQGD YVCLAQDRKT KKRHCVVRQL TVLERVAPTI  TGNLENQTTS IGESIEVSCT ASGNPPPQIM WFKDNETLVE DSGIVLKDGN RNLTIRRVRK EDEGLYTCQA CSVLGCAKVE AFFIIEGANA SDKTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSREEMT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPMLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGK.

Product Science Overview

Introduction

Vascular Endothelial Growth Factor Receptor-2 (VEGFR-2), also known as KDR (Kinase Insert Domain Receptor) or Flk-1 (Fetal Liver Kinase-1), is a critical receptor in the regulation of angiogenesis and vasculogenesis. The VEGFR-2 Fc Chimera (Human Recombinant) is a fusion protein that combines the extracellular domain of VEGFR-2 with the Fc region of human IgG1. This recombinant protein is expressed in mouse myeloma cells (NS0) and is used extensively in research to study the mechanisms of VEGF signaling and its role in various physiological and pathological processes.

Structure and Composition

The VEGFR-2 Fc Chimera is a homodimeric protein that contains the extracellular domain of human VEGFR-2 fused to the Fc portion of human IgG1. The fusion protein is tagged with a 6x histidine sequence to facilitate purification and detection . The predicted molecular weight of the monomer is approximately 110 kDa, but it appears as a 160-170 kDa band under reducing conditions in SDS-PAGE due to glycosylation .

Function and Mechanism

VEGFR-2 is a type I transmembrane receptor tyrosine kinase that plays a pivotal role in the VEGF signaling pathway. It is primarily involved in the regulation of endothelial cell proliferation, migration, and survival. The binding of VEGF to VEGFR-2 triggers receptor dimerization and autophosphorylation, leading to the activation of downstream signaling pathways that promote angiogenesis .

The VEGFR-2 Fc Chimera acts as a decoy receptor by binding to VEGF with high affinity, thereby inhibiting VEGF-mediated signaling. This inhibition is useful in research settings to study the effects of VEGF blockade on endothelial cell function and angiogenesis .

Applications in Research

The VEGFR-2 Fc Chimera is widely used in various research applications, including:

  • Inhibition of VEGF-dependent proliferation: It is used to inhibit the VEGF-dependent proliferation of human umbilical vein endothelial cells (HUVECs), providing insights into the role of VEGF in endothelial cell biology .
  • Angiogenesis studies: By blocking VEGF signaling, researchers can study the effects of VEGF inhibition on angiogenesis in various models of disease, including cancer, diabetic retinopathy, and age-related macular degeneration .
  • Marker for pluripotent hematopoietic stem cells: The VEGFR-2 Fc Chimera is also used as a marker for identifying and isolating pluripotent hematopoietic stem cells .
Storage and Handling

The VEGFR-2 Fc Chimera is typically supplied as a lyophilized powder and should be reconstituted in sterile phosphate-buffered saline (PBS) containing at least 0.1% human or bovine serum albumin. It should be stored at -20°C to -70°C to maintain stability and avoid repeated freeze-thaw cycles .

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